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P15651

- ACADS_RAT

UniProt

P15651 - ACADS_RAT

Protein

Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acads

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.

    Cofactori

    FAD.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei161 – 1611Substrate; via carbonyl oxygen
    Binding sitei297 – 2971FAD1 Publication
    Binding sitei308 – 3081FADBy similarity
    Active sitei392 – 3921Proton acceptor
    Binding sitei393 – 3931Substrate; via amide nitrogen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi152 – 16110FAD1 Publication
    Nucleotide bindingi185 – 1873FAD1 Publication
    Nucleotide bindingi365 – 3695FAD1 Publication
    Nucleotide bindingi394 – 3963FAD1 Publication

    GO - Molecular functioni

    1. acyl-CoA dehydrogenase activity Source: RGD
    2. butyryl-CoA dehydrogenase activity Source: RGD
    3. fatty-acyl-CoA binding Source: RGD
    4. flavin adenine dinucleotide binding Source: RGD

    GO - Biological processi

    1. butyrate catabolic process Source: RGD
    2. fatty acid beta-oxidation Source: RGD
    3. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: RGD
    4. protein homotetramerization Source: RGD
    5. response to glucocorticoid Source: RGD
    6. response to starvation Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    SABIO-RKP15651.
    UniPathwayiUPA00660.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Short-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.1)
    Short name:
    SCAD
    Alternative name(s):
    Butyryl-CoA dehydrogenase
    Gene namesi
    Name:Acads
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620514. Acads.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: BHF-UCL
    2. mitochondrial membrane Source: BHF-UCL
    3. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424MitochondrionAdd
    BLAST
    Chaini25 – 412388Short-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000501Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei51 – 511N6-acetyllysine; alternateBy similarity
    Modified residuei51 – 511N6-succinyllysine; alternateBy similarity
    Modified residuei72 – 721N6-acetyllysineBy similarity
    Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
    Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
    Modified residuei208 – 2081N6-acetyllysineBy similarity
    Modified residuei262 – 2621N6-acetyllysine; alternateBy similarity
    Modified residuei262 – 2621N6-succinyllysine; alternateBy similarity
    Modified residuei292 – 2921N6-acetyllysineBy similarity
    Modified residuei306 – 3061N6-acetyllysine; alternateBy similarity
    Modified residuei306 – 3061N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP15651.
    PRIDEiP15651.

    Expressioni

    Gene expression databases

    GenevestigatoriP15651.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    IntActiP15651. 1 interaction.
    STRINGi10116.ENSRNOP00000001556.

    Structurei

    Secondary structure

    1
    412
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 5217
    Turni53 – 564
    Helixi57 – 637
    Helixi68 – 7710
    Turni78 – 803
    Beta strandi81 – 844
    Helixi86 – 883
    Helixi95 – 10814
    Helixi110 – 12112
    Helixi124 – 1307
    Helixi133 – 1397
    Helixi141 – 1433
    Beta strandi144 – 1474
    Beta strandi150 – 1534
    Beta strandi159 – 1624
    Beta strandi169 – 1724
    Beta strandi174 – 18714
    Turni188 – 1914
    Beta strandi193 – 2019
    Helixi203 – 2086
    Beta strandi209 – 21810
    Beta strandi222 – 2243
    Beta strandi230 – 2323
    Beta strandi238 – 24912
    Helixi250 – 2523
    Beta strandi253 – 2564
    Helixi260 – 29637
    Beta strandi298 – 3036
    Helixi304 – 3063
    Helixi308 – 33629
    Helixi342 – 36726
    Helixi368 – 3714
    Helixi378 – 3858
    Helixi386 – 3894
    Turni390 – 3923
    Helixi395 – 41016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JQIX-ray2.25A/B25-412[»]
    ProteinModelPortaliP15651.
    SMRiP15651. Positions 28-411.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15651.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni269 – 2724Substrate binding

    Sequence similaritiesi

    Belongs to the acyl-CoA dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1960.
    HOVERGENiHBG000224.
    InParanoidiP15651.
    KOiK00248.

    Family and domain databases

    Gene3Di1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProiIPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view]
    PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15651-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAALLARAG GSLGRALRAR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE    50
    KELVPIAAQL DKEHLFPTSQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI 100
    ALEEISRGCA STGVIMSVNN SLYLGPILKF GSSQQKQQWI TPFTNGDKIG 150
    CFALSEPGNG SDAGAASTTA REEGDSWVLN GTKAWITNSW EASATVVFAS 200
    TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN LIFEDCRIPK 250
    ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRHAF 300
    GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL 350
    AASEAATAIS HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL 400
    VIAGHLLRSY RS 412
    Length:412
    Mass (Da):44,765
    Last modified:November 1, 1995 - v2
    Checksum:i3E4A052FC99B8E14
    GO

    Sequence cautioni

    The sequence AAA40669.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05030 mRNA. Translation: AAA40669.1. Different initiation.
    PIRiB34252.
    RefSeqiNP_071957.1. NM_022512.2.
    UniGeneiRn.1167.

    Genome annotation databases

    GeneIDi64304.
    KEGGirno:64304.
    UCSCiRGD:620514. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05030 mRNA. Translation: AAA40669.1 . Different initiation.
    PIRi B34252.
    RefSeqi NP_071957.1. NM_022512.2.
    UniGenei Rn.1167.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JQI X-ray 2.25 A/B 25-412 [» ]
    ProteinModelPortali P15651.
    SMRi P15651. Positions 28-411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P15651. 1 interaction.
    STRINGi 10116.ENSRNOP00000001556.

    Chemistry

    ChEMBLi CHEMBL2176825.

    Proteomic databases

    PaxDbi P15651.
    PRIDEi P15651.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64304.
    KEGGi rno:64304.
    UCSCi RGD:620514. rat.

    Organism-specific databases

    CTDi 35.
    RGDi 620514. Acads.

    Phylogenomic databases

    eggNOGi COG1960.
    HOVERGENi HBG000224.
    InParanoidi P15651.
    KOi K00248.

    Enzyme and pathway databases

    UniPathwayi UPA00660 .
    SABIO-RK P15651.

    Miscellaneous databases

    EvolutionaryTracei P15651.
    NextBioi 612942.
    PROi P15651.

    Gene expression databases

    Genevestigatori P15651.

    Family and domain databases

    Gene3Di 1.10.540.10. 1 hit.
    2.40.110.10. 1 hit.
    InterProi IPR006089. Acyl-CoA_DH_CS.
    IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
    IPR009075. AcylCo_DH/oxidase_C.
    IPR013786. AcylCoA_DH/ox_N.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    [Graphical view ]
    Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
    PF02770. Acyl-CoA_dh_M. 1 hit.
    PF02771. Acyl-CoA_dh_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
    PS00073. ACYL_COA_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family."
      Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K.
      J. Biol. Chem. 264:16321-16331(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases."
      Battaile K.P., Molin-Case J., Paschke R., Wang M., Bennett D., Vockley J., Kim J.-J.P.
      J. Biol. Chem. 277:12200-12207(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 25-412 IN COMPLEX WITH THE SUBSTRATE ANALOG ACETOACETYL-COA AND FAD, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiACADS_RAT
    AccessioniPrimary (citable) accession number: P15651
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3